Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serine/threonine-protein kinase PLK1  

UniProtKB / Swiss-Prot ID :  PLK1_HUMAN

Gene Name (Synonyms) : 
PLK1, PLK  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, centrosome. Cytoplasm, cytoskeleton, spindle. Midbody. Note=During early stages of mitosis, the phosphorylated form is detected on centrosomes and kinetochores. Localizes to the outer 

Protein Function :  Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, MLF1IP, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, PLK1S1/KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGOL1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1 and WEE1. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating PLK1S1/KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, MLF1IP, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, MLF1IP, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatide cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGOL1: required for spindle pole localization of isoform 3 of SGOL1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73- mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. 

Protein Sequence MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEI...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHCCCCCHHHEEEEEEEEECCCEEEEEE...
Protein Variant
LocationDescription
12R -> L (in a lung squamous cell carcinomasample; somatic mutation).
261L -> F (in dbSNP:rs35056440). VAR_041019
297N -> D (in dbSNP:rs16972799). VAR_051659
332L -> V (in dbSNP:rs45489499). VAR_041020
463L -> H (in dbSNP:rs45569335). VAR_041021
518R -> H (in dbSNP:rs56027600). VAR_041022
595S -> L (in dbSNP:rs34001032). VAR_051660
599R -> H (in dbSNP:rs34954545). VAR_051661
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2Phosphoserine---MSAAVT
---CCCCCC
25.57HPRD
Link-
2Phosphoserine---MSAAVT
---CCCCCC
25.57Phosphositeplus
Link-
6PhosphothreonineSAAVTAGKL
CCCCCCCCC
25.60HPRD
Link-
6PhosphothreonineSAAVTAGKL
CCCCCCCCC
25.60Phosphositeplus
Link-
6PhosphothreonineSAAVTAGKL
CCCCCCCCC
25.60SysPTM
Link-
6Phosphothreonine.SAAVTAGKL
CCCCCCCCC
25.60UniProtKB
Link-
38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)APPAKEIPE
CCCCHHHHH
63.05Phosphositeplus
Link-
49PhosphoserineVDPRSRRRY
CCCCCHHHE
35.21Phosphositeplus
Link-
103PhosphoserineSMEISIHRS
HHHHHHHHH
10.07HPRD
Link-
103PhosphoserineSMEISIHRS
HHHHHHHHH
10.07Phosphositeplus
Link-
103PhosphoserineSMEISIHRS
HHHHHHHHH
10.07SysPTM
Link-
103Phosphoserine.SMEISIHRS
HHHHHHHHH
10.07UniProtKB
Link-
137PhosphoserineCRRRSLLEL
CCCCHHHHH
35.18PhosphoELM
Link-
137PhosphoserineCRRRSLLEL
CCCCHHHHH
35.18Phosphositeplus
Link-
200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GLATKVEYD
CEEEEECCC
27.71Phosphositeplus
Link-
210PhosphothreonineERKKTLCGT
CEEEEECCC
30.25HPRD
Link-
210PhosphothreonineERKKTLCGT
CEEEEECCC
30.25Phosphositeplus
Link-
210PhosphothreonineERKKTLCGT
CEEEEECCC
30.25SysPTM
Link-
210Phosphothreonine (LOK)ERKKTLCGT
CEEEEECCC
30.25PhosphoELM
Link-
210Phosphothreonine; by AURKA.ERKKTLCGT
CEEEEECCC
30.25UniProtKB
Link-
214PhosphothreonineTLCGTPNYI
EECCCHHHC
13.83HPRD
Link-
214PhosphothreonineTLCGTPNYI
EECCCHHHC
13.83PhosphoELM
Link-
214PhosphothreonineTLCGTPNYI
EECCCHHHC
13.83Phosphositeplus
Link-
214PhosphothreonineTLCGTPNYI
EECCCHHHC
13.83SysPTM
Link-
214Phosphothreonine.TLCGTPNYI
EECCCHHHC
13.83UniProtKB
Link-
217PhosphotyrosineGTPNYIAPE
CCHHHCCHH
10.32Phosphositeplus
Link-
224PhosphoserinePEVLSKKGH
HHHHCCCCC
37.18Phosphositeplus
Link-
272Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YSIPKHINP
CCCCCCCCH
56.28Phosphositeplus
Link-
326PhosphoserinePPRFSIAPS
CCCCCCCCC
21.08Phosphositeplus
Link-
330PhosphoserineSIAPSSLDP
CCCCCCCCH
34.21HPRD
Link-
330PhosphoserineSIAPSSLDP
CCCCCCCCH
34.21Phosphositeplus
Link-
335PhosphoserineSLDPSNRKP
CCCHHHHHH
49.27Phosphositeplus
Link-
335Phosphoserine.SLDPSNRKP
CCCHHHHHH
49.27UniProtKB
Link-
375PhosphoserineDCHLSDMLQ
HHHHHHHHH
9.41HPRD
Link
375PhosphoserineDCHLSDMLQ
HHHHHHHHH
9.41Phosphositeplus
Link
375PhosphoserineDCHLSDMLQ
HHHHHHHHH
9.41SysPTM
Link
375Phosphoserine.DCHLSDMLQ
HHHHHHHHH
9.41UniProtKB
Link
383PhosphoserineQQLHSVNAS
HHHHHCCCC
26.17Phosphositeplus
Link
387PhosphoserineSVNASKPSE
HCCCCCCCC
39.64HPRD
Link
387PhosphoserineSVNASKPSE
HCCCCCCCC
39.64PhosphoELM
Link
387PhosphoserineSVNASKPSE
HCCCCCCCC
39.64Phosphositeplus
Link
450PhosphoserineNDGDSLQYI
CCCCEEEEE
23.93HPRD
Link
450PhosphoserineNDGDSLQYI
CCCCEEEEE
23.93Phosphositeplus
Link
450PhosphoserineNDGDSLQYI
CCCCEEEEE
23.93SysPTM
Link
450Phosphoserine.NDGDSLQYI
CCCCEEEEE
23.93UniProtKB
Link
461PhosphoserineDGTESYLTV
CCCCCCCCC
25.86HPRD
Link
461PhosphoserineDGTESYLTV
CCCCCCCCC
25.86Phosphositeplus
Link
461PhosphoserineDGTESYLTV
CCCCCCCCC
25.86SysPTM
Link
461Phosphoserine.DGTESYLTV
CCCCCCCCC
25.86UniProtKB
Link
464PhosphothreonineESYLTVSSH
CCCCCCCHH
15.31HPRD
Link
464PhosphothreonineESYLTVSSH
CCCCCCCHH
15.31Phosphositeplus
Link
464PhosphothreonineESYLTVSSH
CCCCCCCHH
15.31SysPTM
Link
464Phosphothreonine.ESYLTVSSH
CCCCCCCHH
15.31UniProtKB
Link
474Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NSLMKKITL
HHHCCCCHH
46.44Phosphositeplus
Link
480Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ITLLKYFRN
CHHHHHHHH
45.51Phosphositeplus
Link
492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EHLLKAGAN
HHHHHHCCC
51.65Phosphositeplus
Link
498PhosphothreonineGANITPREG
CCCCCCCCC
18.99HPRD
Link
498PhosphothreonineGANITPREG
CCCCCCCCC
18.99Phosphositeplus
Link
498PhosphothreonineGANITPREG
CCCCCCCCC
18.99SysPTM
Link
498Phosphothreonine.GANITPREG
CCCCCCCCC
18.99UniProtKB
Link
589Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TMVDKLLSS
HHHHHHHHH
39.66Phosphositeplus
Link
597PhosphoserineSRSASNRLK
HHHHHHHHC
24.59Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RECQ5_HUMANphysical interactionMINT-63234MINT16169070
P53_HUMANphysical interactionMINT-2634822MINT16753148
P53_HUMANphysical interactionMINT-2634842MINT16753148
P53_HUMANphysical interactionMINT-2634880MINT16753148
MPIP3_HUMANphysical interactionMINT-50542MINT14532005
PLK1_HUMANphysical interactionMINT-50543MINT14532005
PIN1_HUMANphysical interactionMINT-15021MINT10037602
CG020_HUMANphysical interactionMINT-65704MINT16169070
CHK2_HUMANcolocalization
phosphorylation
phosphorylation
physical interaction
physical interaction
physical interaction
EBI-1215154
EBI-1215133
EBI-1
intact12493754
12493754
12493754
12493754
12493754
12493754
MCM2_HUMANphysical interactionEBI-476798
intact15654075
FBX5_HUMANphosphorylationEBI-866028
intact16439210
MCM2_HUMANin vivoHPRD:03652HPRD15654075
CCNB1_HUMANin vivoHPRD:03652HPRD11242082
PSA3_HUMANin vivoHPRD:03652HPRD11205743
PSA5_HUMANin vivoHPRD:03652HPRD11205743
MPIP3_HUMANin vitro
in vivo
HPRD:03652HPRD11202906
12595692
11897663
16753148
NPM_HUMANin vitro
in vivo
HPRD:03652HPRD15190079
MCM7_HUMANin vitro
in vivo
HPRD:03652HPRD15654075
TBA4A_HUMANin vitro
in vivo
HPRD:03652HPRD10191277
TBB5_HUMANin vitro
in vivo
HPRD:03652HPRD10191277
TBG1_HUMANin vitro
in vivo
HPRD:03652HPRD10191277
DNJB9_HUMANyeast 2-hybridHPRD:03652HPRD16169070
BRCA2_HUMANin vitro
in vivo
HPRD:03652HPRD12815053
PIN1_HUMANin vitroHPRD:03652HPRD9499405
16118204
PSB5_HUMANin vivoHPRD:03652HPRD11205743
PSB6_HUMANin vivoHPRD:03652HPRD11205743
MYT1_HUMANin vitroHPRD:03652HPRD12738781
PSB1_HUMANin vivoHPRD:03652HPRD11205743
PMYT1_HUMANin vitroHPRD:03652HPRD12738781
CHK2_HUMANin vitro
in vivo
HPRD:03652HPRD12493754
11901158
12242661
10973490
12024051
NUDC_HUMANin vitro
in vivo
HPRD:03652HPRD12852857
TCTP_HUMANin vitro
in vivo
HPRD:03652HPRD12167714
WEE1_HUMANin vitroHPRD:03652HPRD15070733
MAGD1_HUMANyeast 2-hybridHPRD:03652HPRD16169070
RECQ5_HUMANyeast 2-hybridHPRD:03652HPRD16169070
CG020_HUMANyeast 2-hybridHPRD:03652HPRD16169070
ECT2_HUMANin vitroHPRD:03652HPRD16247472
BUB1_HUMANin vitro
in vivo
HPRD:03652HPRD16760428
CDC27_HUMANENSP00000300093STRING
UB2D1_HUMANENSP00000300093STRING
CDC23_HUMANENSP00000300093STRING
FBX5_HUMANENSP00000300093STRING
KI20A_HUMANENSP00000300093STRING
CDN1A_HUMANENSP00000300093STRING
PIN1_HUMANENSP00000300093STRING
PIN1_HUMANENSP00000300093STRING
CCNB1_HUMANENSP00000300093STRING
KIF23_HUMANENSP00000300093STRING
ANC5_HUMANENSP00000300093STRING
PMYT1_HUMANENSP00000300093STRING
P53_HUMANENSP00000300093STRING
BUB1B_HUMANENSP00000300093STRING
CCNB2_HUMANENSP00000300093STRING
RAD21_HUMANENSP00000300093STRING
WEE1_HUMANENSP00000300093STRING
BUB1_HUMANENSP00000300093STRING
UB2E1_HUMANENSP00000300093STRING
CDC2_HUMANENSP00000300093STRING
CDC20_HUMANENSP00000300093STRING
REC8_HUMANENSP00000300093STRING
REC8_HUMANENSP00000300093STRING
APC10_HUMANENSP00000300093STRING
GR65_HUMANENSP00000300093STRING
AURKB_HUMANENSP00000300093STRING
ANC2_HUMANENSP00000300093STRING
ANC4_HUMANENSP00000300093STRING
STK6_HUMANENSP00000300093STRING
MPIP3_HUMANENSP00000300093STRING
SMC1A_HUMANENSP00000300093STRING
CHK2_HUMANENSP00000300093STRING
ANC1_HUMANENSP00000300093STRING
APC11_HUMANENSP00000300093STRING
PTTG1_HUMANENSP00000300093STRING
PTTG2_HUMANENSP00000300093STRING
APC7_HUMANENSP00000300093STRING
CDC16_HUMANENSP00000300093STRING
SMC3_HUMANENSP00000300093STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation of threonine 210 and the role of serine 137 in theregulation of mammalian polo-like kinase.";
Jang Y.-J., Ma S., Terada Y., Erikson R.L.;
J. Biol. Chem. 277:44115-44120(2002).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-137 AND THR-210, AND MUTAGENESIS OFLYS-82; SER-137 AND THR-210.
"Identification of phosphorylation sites in the polo-like kinases Plx1and Plk1 by a novel strategy based on element and electrospray highresolution mass spectrometry.";
Wind M., Kelm O., Nigg E.A., Lehmann W.D.;
Proteomics 2:1516-1523(2002).
Cited for: PHOSPHORYLATION AT SER-335.
"Myosin phosphatase-targeting subunit 1 regulates mitosis byantagonizing polo-like kinase 1.";
Yamashiro S., Yamakita Y., Totsukawa G., Goto H., Kaibuchi K., Ito M.,Hartshorne D.J., Matsumura F.;
Dev. Cell 14:787-797(2008).
Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A, PHOSPHORYLATION AT THR-210,DEPHOSPHORYLATION BY PPP1C, SUBCELLULAR LOCATION, AND MUTAGENESIS OFHIS-538 AND LYS-540.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-103; THR-210;THR-214; SER-375; SER-450; SER-461; THR-464 AND THR-498, AND MASSSPECTROMETRY.
"Polo-like kinase-1 is activated by aurora A to promote checkpointrecovery.";
Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R.,Freire R., Clouin C., Taylor S.S., Yaffe M.B., Medema R.H.;
Nature 455:119-123(2008).
Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-210 BY AURKA,SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-82; SER-137; ASP-176 ANDTHR-210.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures